We have performed cocrystallization with ligands, however, no esterase Rv0045c-substrate complex has been successfully crystallized by now. We will continue to seek the way to get solvable crystals of Rv004c-substrate complex to clarify the catalytic mechanism of Rv0045c. Tuberculosis is a contagious respiratory system disease, which is caused by M. tuberculosis via infecting the lungs of mammalian. M. tuberculosis can BI-9564 tolerate and withstand rigorous condition and weak disinfectants to survive in a dry state for weeks. It was reported that the unusual cell wall, rich in lipids, is likely responsible for this resistance. Rv0045c is proposed to be an esterase or hydrolase involved in lipid metabolism. Our study determines for the first time the structure of Rv0045c and will give further insight into the mechanism of esters or lipids hydrolysis in M. tuberculosis. This work will help to design and screen inhibitors against to verify the function and role of this enzyme in M. tuberculosis. Voltage-dependent anion channel, as a membrane channel protein, is firstly identified in the mitochondrial outer membrane of Paramecium Aurelia. It has now been discovered in the mitochondrial outer membrane of most eukaryotes. VDAC is highly conserved in molecular structure and function during evolution. In mammals, three homologous genes encode and express three corresponding protein subtypes with similar molecular weight, each of them shares approximately 70% identity to the others. Current studies show that the most abundant subtype is VDAC1 and that the least common form is VDAC3. VDAC1 and VDAC2 can form the channel structure across the artificial lipid bilayer in vitro, but VDAC3 does not easily incorporate in the reconstituted membrane. VDAC in the mitochondrial outer membrane can regulate membrane permeability to small ions and molecules according to membrane potential changes. Therefore, VDAC is reportedly involved in many mitochondria-related biological processes, such as energy metabolism and cell apoptosis. VDAC is once Povidone iodine thought to be only localized in the mitochondrial outer membrane. However this protein is recently found in the plasma membrane or other non-mitochondrial cellular components, which implies that VDAC has more novel functions.